메뉴 건너뛰기




Volumn 11, Issue 5, 2000, Pages 1753-1764

The yeast heat shock transcription factor changes conformation in response to superoxide and temperature

Author keywords

[No Author keywords available]

Indexed keywords

DNA; HEAT SHOCK PROTEIN; SUPEROXIDE; TRANSCRIPTION FACTOR;

EID: 0034108630     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.11.5.1753     Document Type: Article
Times cited : (49)

References (59)
  • 1
    • 0026665975 scopus 로고
    • The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression
    • Abravaya, K., Myers, M.P., Murphy, S.P., and Morimoto, R.I. (1992). The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression. Genes Dev. 6, 1153-1164.
    • (1992) Genes Dev. , vol.6 , pp. 1153-1164
    • Abravaya, K.1    Myers, M.P.2    Murphy, S.P.3    Morimoto, R.I.4
  • 2
    • 0027938515 scopus 로고
    • Cooperative binding of heat shock transcription factor to the Hsp70 promoter in vivo and in vitro
    • Amin, J., Fernandez, M., Ananthan, J., Lis, J.T., and Voellmy, R. (1994). Cooperative binding of heat shock transcription factor to the Hsp70 promoter in vivo and in vitro. J. Biol. Chem. 269, 4804-4811.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4804-4811
    • Amin, J.1    Fernandez, M.2    Ananthan, J.3    Lis, J.T.4    Voellmy, R.5
  • 3
    • 0027474909 scopus 로고
    • Activation of human heat shock genes is accompanied by oligomerization, modification, and rapid translocation of heat shock transcription factor HSF1
    • Baler, R., Dahl, G., and Voellmy, R. (1993). Activation of human heat shock genes is accompanied by oligomerization, modification, and rapid translocation of heat shock transcription factor HSF1. Mol. Cell. Biol. 13, 2486-2496.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2486-2496
    • Baler, R.1    Dahl, G.2    Voellmy, R.3
  • 4
    • 0026750001 scopus 로고
    • Heat shock gene regulation by nascent polypeptides and denatured proteins: Hsp70 as a potential autoregulatory factor
    • Baler, R., Welch, W.J., and Voellmy, R. (1992). Heat shock gene regulation by nascent polypeptides and denatured proteins: hsp70 as a potential autoregulatory factor. J. Cell Biol. 117, 1151-1159.
    • (1992) J. Cell Biol. , vol.117 , pp. 1151-1159
    • Baler, R.1    Welch, W.J.2    Voellmy, R.3
  • 5
    • 0030112452 scopus 로고    scopus 로고
    • Evidence for a role of Hsp70 in the regulation of the heat shock response in mammalian cells
    • Baler, R., Zou, J., and Voellmy, R. (1996). Evidence for a role of Hsp70 in the regulation of the heat shock response in mammalian cells. Cell Stress Chaperones 1, 33-39.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 33-39
    • Baler, R.1    Zou, J.2    Voellmy, R.3
  • 6
    • 0032476044 scopus 로고    scopus 로고
    • Superoxide dependence of the toxicity of short chain sugars
    • Benov, L., and Fridovich, I. (1998). Superoxide dependence of the toxicity of short chain sugars. J. Biol. Chem. 273, 25741-25744.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25741-25744
    • Benov, L.1    Fridovich, I.2
  • 7
    • 0025799905 scopus 로고
    • Vectors for the expression and analysis of DNA-binding proteins in yeast
    • Bonner, J.J. (1991). Vectors for the expression and analysis of DNA-binding proteins in yeast. Gene 104, 113-118.
    • (1991) Gene , vol.104 , pp. 113-118
    • Bonner, J.J.1
  • 8
    • 0028047311 scopus 로고
    • Interactions between DNA-bound trimers of the yeast heat shock factor
    • Bonner, J.J., Ballou, C., and Fackenthal, D.L. (1994). Interactions between DNA-bound trimers of the yeast heat shock factor. Mol. Cell. Biol. 14, 501-508.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 501-508
    • Bonner, J.J.1    Ballou, C.2    Fackenthal, D.L.3
  • 10
    • 0026526179 scopus 로고
    • Temperature-dependent regulation of a heterologous transcriptional activation domain fused to yeast heat shock transcription factor
    • Bonner, J.J., Heyward, S., and Fackenthal, D.L. (1992). Temperature-dependent regulation of a heterologous transcriptional activation domain fused to yeast heat shock transcription factor. Mol. Cell. Biol. 12, 1021-1030.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1021-1030
    • Bonner, J.J.1    Heyward, S.2    Fackenthal, D.L.3
  • 11
    • 0021736624 scopus 로고
    • Stimuli that induce a yeast heat shock gene fused to beta-galactosidase
    • Brazzell, C., and Ingolia, T.D. (1984). Stimuli that induce a yeast heat shock gene fused to beta-galactosidase. Mol. Cell. Biol. 4, 2573-2579.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 2573-2579
    • Brazzell, C.1    Ingolia, T.D.2
  • 13
    • 0029763452 scopus 로고    scopus 로고
    • Transcriptional repression of the prointerleukin 1β gene by heat shock factor 1
    • Cahill, C.M., Waterman, W.R., Xie, Y., Auron, P.E, and Calderwood, S.K. (1996). Transcriptional repression of the prointerleukin 1β gene by heat shock factor 1. J. Biol. Chem. 271, 24874-24879.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24874-24879
    • Cahill, C.M.1    Waterman, W.R.2    Xie, Y.3    Auron, P.E.4    Calderwood, S.K.5
  • 15
    • 0032789981 scopus 로고    scopus 로고
    • A role for RNA metabolism in inducing the heat shock response
    • Carlson, T., Christian, N., and Bonner, J.J. (1999). A role for RNA metabolism in inducing the heat shock response. Gene Expr. 7, 283-292.
    • (1999) Gene Expr. , vol.7 , pp. 283-292
    • Carlson, T.1    Christian, N.2    Bonner, J.J.3
  • 16
    • 0027491654 scopus 로고
    • Identification of the C-terminal activator domain in yeast heat shock factor: Independent control of transient and sustained transcriptional activity
    • Chen, Y., Barlev, N.A., Westergaard, O., and Jakobsen, B.K. (1993). Identification of the C-terminal activator domain in yeast heat shock factor: independent control of transient and sustained transcriptional activity. EMBO J. 12, 5007-5018.
    • (1993) EMBO J. , vol.12 , pp. 5007-5018
    • Chen, Y.1    Barlev, N.A.2    Westergaard, O.3    Jakobsen, B.K.4
  • 17
    • 0024298718 scopus 로고
    • Periodic interactions of heat shock transcriptional elements
    • Cohen, R.S., and Meselson, M. (1988). Periodic interactions of heat shock transcriptional elements. Nature 332, 856-858.
    • (1988) Nature , vol.332 , pp. 856-858
    • Cohen, R.S.1    Meselson, M.2
  • 18
    • 0023655407 scopus 로고
    • Protein damage and degradation by oxygen radicals. II. Modification of amino acids
    • Davies, K., Delsignore, M.E., and Lin, S.W. (1987). Protein damage and degradation by oxygen radicals. II. Modification of amino acids. J. Biol. Chem. 262, 9902-9907.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9902-9907
    • Davies, K.1    Delsignore, M.E.2    Lin, S.W.3
  • 19
    • 0028352287 scopus 로고
    • Yeast heat shock transcription factor contains a flexible linker between the DNA-binding and trimerization domains - Implications for DNA binding by trimeric proteins
    • Flick, K.E., Gonzalez, L., Harrison, C.J., and Nelson, H.C.M. (1994). Yeast heat shock transcription factor contains a flexible linker between the DNA-binding and trimerization domains - implications for DNA binding by trimeric proteins. J. Biol. Chem. 269, 12475-12481.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12475-12481
    • Flick, K.E.1    Gonzalez, L.2    Harrison, C.J.3    Nelson, H.C.M.4
  • 20
    • 0028911832 scopus 로고
    • Dynamic protein-DNA architecture of a yeast heat shock promoter
    • Giardina, C., and Lis, J.T. (1995). Dynamic protein-DNA architecture of a yeast heat shock promoter. Mol. Cell. Biol. 15, 2737-2744.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2737-2744
    • Giardina, C.1    Lis, J.T.2
  • 21
    • 0027319565 scopus 로고
    • Protein-bound 3,4-dihydroxyphenylalanine is a major reductant formed during hydroxyl radical damage to proteins
    • Gieseg, S.P., Simpson, J.A., Charlton, T.S., Duncan, M.W., and Dean, R.T. (1993). Protein-bound 3,4-dihydroxyphenylalanine is a major reductant formed during hydroxyl radical damage to proteins. Biochemistry 32, 4780-4786.
    • (1993) Biochemistry , vol.32 , pp. 4780-4786
    • Gieseg, S.P.1    Simpson, J.A.2    Charlton, T.S.3    Duncan, M.W.4    Dean, R.T.5
  • 22
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz, R.D., and Sugino, A. (1988). New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 74, 527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 23
    • 0015459047 scopus 로고
    • The role of superoxide radical in a nonenzymatic hydroxylation
    • Goscin, S.A., and Fridovich, I. (1972). The role of superoxide radical in a nonenzymatic hydroxylation. Arch. Biochem. Biophys. 153, 778-783.
    • (1972) Arch. Biochem. Biophys. , vol.153 , pp. 778-783
    • Goscin, S.A.1    Fridovich, I.2
  • 25
    • 0025678738 scopus 로고
    • Genomic footprinting of the yeast HSP82 promoter reveals marked distortion of the DNA helix and constitutive occupancy of heat shock and TATA elements
    • Gross, D.S., English, K.E., Collins, K.W., and Lee, S.W. (1990). Genomic footprinting of the yeast HSP82 promoter reveals marked distortion of the DNA helix and constitutive occupancy of heat shock and TATA elements. J. Mol. Biol. 216, 611-631.
    • (1990) J. Mol. Biol. , vol.216 , pp. 611-631
    • Gross, D.S.1    English, K.E.2    Collins, K.W.3    Lee, S.W.4
  • 26
    • 0027958045 scopus 로고
    • Crystal structure of the DNA binding domain of the heat shock transcription factor
    • Harrison, C.J., Bohm, A.A., and Nelson, H.C.M. (1994). Crystal structure of the DNA binding domain of the heat shock transcription factor. Science 263, 224-227.
    • (1994) Science , vol.263 , pp. 224-227
    • Harrison, C.J.1    Bohm, A.A.2    Nelson, H.C.M.3
  • 27
    • 0028321786 scopus 로고
    • A short element required for turning off heat shock transcription factor: Evidence that phosphorylation enhances deactivation
    • Høj, A., and Jakobsen, B.K. (1994). A short element required for turning off heat shock transcription factor: evidence that phosphorylation enhances deactivation. EMBO J. 13, 2617-2624.
    • (1994) EMBO J. , vol.13 , pp. 2617-2624
    • Høj, A.1    Jakobsen, B.K.2
  • 28
    • 0023701108 scopus 로고
    • Constitutive binding of yeast heat shock factor to DNA in vivo
    • Jakobsen, B.K., and Pelham, H.R. (1988). Constitutive binding of yeast heat shock factor to DNA in vivo. Mol. Cell. Biol. 8, 5040-5042.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 5040-5042
    • Jakobsen, B.K.1    Pelham, H.R.2
  • 29
    • 0025974219 scopus 로고
    • Tackling the protease problem in yeast
    • Jones, E.W. (1991). Tackling the protease problem in yeast. Methods Enzymol. 194, 428-453.
    • (1991) Methods Enzymol. , vol.194 , pp. 428-453
    • Jones, E.W.1
  • 30
    • 0027113344 scopus 로고
    • Effect of sodium salicylate on the human heat shock response
    • Jurivich, D.A., Sistonen, L., Kroes, R.A., and Morimoto, R.I. (1992). Effect of sodium salicylate on the human heat shock response. Science 255, 1243-1245.
    • (1992) Science , vol.255 , pp. 1243-1245
    • Jurivich, D.A.1    Sistonen, L.2    Kroes, R.A.3    Morimoto, R.I.4
  • 31
    • 0026739631 scopus 로고
    • Translational readthrough at nonsense mutations in the HSF1 gene of Saccharomyces cerevisiae
    • Kopczynski, J.B., Raff, A.C., and Bonner, J.J. (1992). Translational readthrough at nonsense mutations in the HSF1 gene of Saccharomyces cerevisiae. Mol. Gen. Genet. 234, 369-378.
    • (1992) Mol. Gen. Genet. , vol.234 , pp. 369-378
    • Kopczynski, J.B.1    Raff, A.C.2    Bonner, J.J.3
  • 32
    • 0032936785 scopus 로고    scopus 로고
    • A new use for the "wing" of the "winged" helix-turn-helix motif in the HSF-DNA cocrystal
    • Littlefield, O., and Nelson, H.C.M. (1999). A new use for the "wing" of the "winged" helix-turn-helix motif in the HSF-DNA cocrystal. Nat. Struct. Biol. 6, 464-470.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 464-470
    • Littlefield, O.1    Nelson, H.C.M.2
  • 33
    • 0029664413 scopus 로고    scopus 로고
    • Oxidative stress induces heat shock factor phosphorylation and HSF-dependent activation of yeast metallothionein gene transcription
    • Liu, X.-D., and Thiele, D.J. (1996). Oxidative stress induces heat shock factor phosphorylation and HSF-dependent activation of yeast metallothionein gene transcription. Genes Dev. 10, 592-603.
    • (1996) Genes Dev. , vol.10 , pp. 592-603
    • Liu, X.-D.1    Thiele, D.J.2
  • 34
    • 0025300038 scopus 로고
    • In vitro activation of heat shock transcription factor DNA-binding by calcium and biochemical conditions that affect protein conformation
    • Mosser, D.D., Kotzbauer, P.T., Sarge, K.D., and Morimoto, R.I. (1990). In vitro activation of heat shock transcription factor DNA-binding by calcium and biochemical conditions that affect protein conformation. Proc. Natl. Acad. Sci. USA 87: 3748-3752.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3748-3752
    • Mosser, D.D.1    Kotzbauer, P.T.2    Sarge, K.D.3    Morimoto, R.I.4
  • 35
    • 0025122831 scopus 로고
    • The yeast heat shock transcription factor contains a transcriptional activation domain whose activity is repressed under nonshock conditions
    • Nieto-Sotelo, J., Wiederrecht, G., Okuda, A., and Parker, C.S. (1990). The yeast heat shock transcription factor contains a transcriptional activation domain whose activity is repressed under nonshock conditions. Cell 62, 807-817.
    • (1990) Cell , vol.62 , pp. 807-817
    • Nieto-Sotelo, J.1    Wiederrecht, G.2    Okuda, A.3    Parker, C.S.4
  • 36
    • 0023306058 scopus 로고
    • Expression of heat shock genes in homologous and heterologous systems
    • Nover, L. (1987). Expression of heat shock genes in homologous and heterologous systems. Enzyme Microb. Technol. 9, 129-192.
    • (1987) Enzyme Microb. Technol. , vol.9 , pp. 129-192
    • Nover, L.1
  • 37
    • 0019331589 scopus 로고
    • Degradation of deoxyribonucleic acid by a 1, 10-phenanthroline-copper complex: The role of hydroxyl radicals
    • Que, G.G., Downey, K.M., and So, A.G. (1980). Degradation of deoxyribonucleic acid by a 1, 10-phenanthroline-copper complex: the role of hydroxyl radicals. Biochemistry 39, 5987-5991.
    • (1980) Biochemistry , vol.39 , pp. 5987-5991
    • Que, G.G.1    Downey, K.M.2    So, A.G.3
  • 38
    • 0027452754 scopus 로고
    • Regulation of heat shock factor trimer formation: Role of a conserved leucine zipper
    • Rabindran, S.K., Haroun, R.I., Clos, J., Wisniewski, J., and Wu, C. (1993). Regulation of heat shock factor trimer formation: role of a conserved leucine zipper. Science 259, 230-234.
    • (1993) Science , vol.259 , pp. 230-234
    • Rabindran, S.K.1    Haroun, R.I.2    Clos, J.3    Wisniewski, J.4    Wu, C.5
  • 39
    • 34250561475 scopus 로고
    • A new puffing pattern induced by heat shock and DNP in Drosophila
    • Ritossa, F.M. (1962). A new puffing pattern induced by heat shock and DNP in Drosophila. Experientia 18, 571-573.
    • (1962) Experientia , vol.18 , pp. 571-573
    • Ritossa, F.M.1
  • 40
    • 0004915153 scopus 로고
    • Experimental activation of specific loci in polytene chromosomes of Drosophila
    • Ritossa, F.M. (1964). Experimental activation of specific loci in polytene chromosomes of Drosophila. Exp. Cell Res. 35, 601-607.
    • (1964) Exp. Cell Res. , vol.35 , pp. 601-607
    • Ritossa, F.M.1
  • 42
    • 0031771494 scopus 로고    scopus 로고
    • Heat shock element architecture is an important determinant in the temperature and transactivation domain requirements for heat shock transcription factor
    • Santoro, N., Johansson, N., and Thiele, D.J. (1998). Heat shock element architecture is an important determinant in the temperature and transactivation domain requirements for heat shock transcription factor. Mol. Cell. Biol. 18, 6340-6352.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6340-6352
    • Santoro, N.1    Johansson, N.2    Thiele, D.J.3
  • 43
    • 0028886503 scopus 로고
    • Mutated yeast heat shock transcription factor exhibits elevated basal transcriptional activation and confers metal resistance
    • Sewell, A.K., Yokoya, F., Yu, W., Miyawaga, T., Murayama, T., and Winge, D.R. (1995). Mutated yeast heat shock transcription factor exhibits elevated basal transcriptional activation and confers metal resistance. J. Biol. Chem. 270, 25079-25086.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25079-25086
    • Sewell, A.K.1    Yokoya, F.2    Yu, W.3    Miyawaga, T.4    Murayama, T.5    Winge, D.R.6
  • 44
  • 45
    • 0032031725 scopus 로고    scopus 로고
    • Molecular chaperones as HSF1-specific transcriptional repressors
    • Shi, Y., Mosser, D.D., and Morimoto, R.I. (1998). Molecular chaperones as HSF1-specific transcriptional repressors. Genes Dev. 12, 654-666.
    • (1998) Genes Dev. , vol.12 , pp. 654-666
    • Shi, Y.1    Mosser, D.D.2    Morimoto, R.I.3
  • 46
    • 0024989583 scopus 로고
    • Yeast heat shock factor contains separable transient and sustained response transcriptional activators
    • Sorger, P.K. (1990). Yeast heat shock factor contains separable transient and sustained response transcriptional activators. Cell 62, 793-805.
    • (1990) Cell , vol.62 , pp. 793-805
    • Sorger, P.K.1
  • 47
    • 0023643235 scopus 로고
    • Heat shock factor is regulated differently in yeast and HeLa cells
    • Sorger, P.K., Lewis, M.J., and Pelham, H.R.B. (1987). Heat shock factor is regulated differently in yeast and HeLa cells. Nature 329, 81-84.
    • (1987) Nature , vol.329 , pp. 81-84
    • Sorger, P.K.1    Lewis, M.J.2    Pelham, H.R.B.3
  • 48
    • 0024852809 scopus 로고
    • Trimerization of a yeast transcriptional activator via a coiled-coil motif
    • Sorger, P.K., and Nelson, H.C. (1989). Trimerization of a yeast transcriptional activator via a coiled-coil motif. Cell 59, 807-813.
    • (1989) Cell , vol.59 , pp. 807-813
    • Sorger, P.K.1    Nelson, H.C.2
  • 49
    • 0024282785 scopus 로고
    • Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation
    • Sorger, P.K., and Pelham, H.R. (1988). Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation. Cell 54, 855-864.
    • (1988) Cell , vol.54 , pp. 855-864
    • Sorger, P.K.1    Pelham, H.R.2
  • 50
    • 0022272177 scopus 로고
    • Monosaccharide autoxidation in health and disease
    • Thornalley, P.J. (1985). Monosaccharide autoxidation in health and disease. Environ. Health Perspect. 64, 297-307.
    • (1985) Environ. Health Perspect. , vol.64 , pp. 297-307
    • Thornalley, P.J.1
  • 51
    • 0021700982 scopus 로고
    • The production of free radicals during the autoxidation of monosaccharides by buffer ions
    • Thornalley, P.J., and Stern, A. (1984). The production of free radicals during the autoxidation of monosaccharides by buffer ions. Carbohydr. Res. 134, 191-204.
    • (1984) Carbohydr. Res. , vol.134 , pp. 191-204
    • Thornalley, P.J.1    Stern, A.2
  • 52
    • 0021361665 scopus 로고
    • The autoxidation of glyceraldehyde and other simple monosaccharides under physiological conditions catalyzed by buffer ions
    • Thornalley, P.J., Wolff, S., Crabbe, J., and Stern, A. (1984). The autoxidation of glyceraldehyde and other simple monosaccharides under physiological conditions catalyzed by buffer ions. Biochim. Biophys. Acta 797, 276-287.
    • (1984) Biochim. Biophys. Acta , vol.797 , pp. 276-287
    • Thornalley, P.J.1    Wolff, S.2    Crabbe, J.3    Stern, A.4
  • 53
    • 0029117426 scopus 로고
    • Genetic identification of the site of DNA contact in the yeast heat shock transcription factor
    • Torres, F.A.G., and Bonner, J.J. (1995). Genetic identification of the site of DNA contact in the yeast heat shock transcription factor. Mol. Cell. Biol. 15, 5063-5070.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5063-5070
    • Torres, F.A.G.1    Bonner, J.J.2
  • 54
    • 0028500990 scopus 로고
    • Solution structure of the DNA-binding domain of Drosophila heat shock transcription factor
    • Vuister, G.W., Kim, S.-J., Orosz, A., Marquardt, J., Wu, C., and Bax, A. (1994). Solution structure of the DNA-binding domain of Drosophila heat shock transcription factor. Nat. Struct. Biol. 1, 605-614.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 605-614
    • Vuister, G.W.1    Kim, S.-J.2    Orosz, A.3    Marquardt, J.4    Wu, C.5    Bax, A.6
  • 55
    • 0027159173 scopus 로고
    • Activation of Drosophila heat shock factor: Conformational change associated with a monomer-to-trimer transition
    • Westwood, J.T., and Wu, C. (1993). Activation of Drosophila heat shock factor: conformational change associated with a monomer-to-trimer transition. Mol. Cell. Biol. 13, 3481-3486.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3481-3486
    • Westwood, J.T.1    Wu, C.2
  • 57
    • 0032112367 scopus 로고    scopus 로고
    • Direct sensing of heat and oxidation by Drosophila heat shock transcription factor
    • Zhong, M., Orosz, A., and Wu, C. (1998). Direct sensing of heat and oxidation by Drosophila heat shock transcription factor. Mol. Cell 2, 101-108.
    • (1998) Mol. Cell , vol.2 , pp. 101-108
    • Zhong, M.1    Orosz, A.2    Wu, C.3
  • 58
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
    • Zuo, J., Guo, Y., Guettouche, T., Smith, D.F., and Voellmy, R. (1998). Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 94, 471-480.
    • (1998) Cell , vol.94 , pp. 471-480
    • Zuo, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5
  • 59
    • 0028150986 scopus 로고
    • Activation of the DNA-binding ability of human heat shock transcription factor 1 may involve the transition from an intramolecular to an intermolecular triple-stranded coiled-coil structure
    • Zuo, J., Baler, R., Dahl, G., and Voellmy, R. (1994). Activation of the DNA-binding ability of human heat shock transcription factor 1 may involve the transition from an intramolecular to an intermolecular triple-stranded coiled-coil structure. Mol. Cell. Biol. 14, 7557-7568.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7557-7568
    • Zuo, J.1    Baler, R.2    Dahl, G.3    Voellmy, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.